PCID2_HUMAN - dbPTM
PCID2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCID2_HUMAN
UniProt AC Q5JVF3
Protein Name PCI domain-containing protein 2
Gene Name PCID2
Organism Homo sapiens (Human).
Sequence Length 399
Subcellular Localization
Protein Description Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (By similarity). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. [PubMed: 22307388 The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability. R-loop accumulation does not increase in PCID2-depleted cells.]
Protein Sequence MAHITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHRSSQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHEAFFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQCILANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4 (in isoform 2)Phosphorylation-2.7624043423
14 (in isoform 4)Phosphorylation-8.7027642862
24PhosphorylationIDSRDGASCAELVSF
HHCCCCCCHHHHHHC		21.2725850435
32UbiquitinationCAELVSFKHPHVANP
HHHHHHCCCCCCCCC		49.04-
32 (in isoform 4)Ubiquitination-49.04-
45PhosphorylationNPRLQMASPEEKCQQ
CCCCCCCCHHHHHHH		27.7421815630
45 (in isoform 4)Phosphorylation-27.7427251275
49UbiquitinationQMASPEEKCQQVLEP
CCCCHHHHHHHHHCC		35.36-
49 (in isoform 4)Ubiquitination-35.36-
105 (in isoform 3)Ubiquitination-2.1921890473
109PhosphorylationNWALPVMYAVALDLR
CCHHHHHHHHHHHHH		9.7322210691
126 (in isoform 2)Ubiquitination-5.18-
1282-HydroxyisobutyrylationNADQQLVKKGKSKVG
CHHHHHHHCCCCHHH		65.48-
128 (in isoform 1)Ubiquitination-65.4821890473
128 (in isoform 2)Ubiquitination-65.4821890473
128UbiquitinationNADQQLVKKGKSKVG
CHHHHHHHCCCCHHH		65.4821906983
129UbiquitinationADQQLVKKGKSKVGD
HHHHHHHCCCCHHHH		65.18-
133AcetylationLVKKGKSKVGDMLEK
HHHCCCCHHHHHHHH		54.4421466224
133UbiquitinationLVKKGKSKVGDMLEK
HHHCCCCHHHHHHHH		54.44-
178 (in isoform 3)Ubiquitination-3.7121890473
181UbiquitinationQLFKIYFKINKLHLC
HHHHHHHHHCCHHHC		28.53-
182 (in isoform 4)Ubiquitination-3.8421890473
184UbiquitinationKIYFKINKLHLCKPL
HHHHHHCCHHHCHHH		40.53-
187 (in isoform 4)Ubiquitination-6.10-
189AcetylationINKLHLCKPLIRAID
HCCHHHCHHHHHHHC		49.5825953088
189UbiquitinationINKLHLCKPLIRAID
HCCHHHCHHHHHHHC		49.58-
190 (in isoform 3)Ubiquitination-31.8321890473
199 (in isoform 2)Ubiquitination-55.87-
201UbiquitinationAIDSSNLKDDYSTAQ
HHCCCCCCCCCCCCH		53.4521890473
201 (in isoform 2)Ubiquitination-53.4521890473
201 (in isoform 1)Ubiquitination-53.4521890473
201AcetylationAIDSSNLKDDYSTAQ
HHCCCCCCCCCCCCH		53.4526051181
204PhosphorylationSSNLKDDYSTAQRVT
CCCCCCCCCCCHHHH		20.32-
211 (in isoform 2)Ubiquitination-19.24-
213UbiquitinationTAQRVTYKYYVGRKA
CCHHHHHHHHCCCHH		22.272189047
213 (in isoform 1)Ubiquitination-22.2721890473
213AcetylationTAQRVTYKYYVGRKA
CCHHHHHHHHCCCHH		22.2726051181
219MethylationYKYYVGRKAMFDSDF
HHHHCCCHHHCCCCH		37.9782984321
219UbiquitinationYKYYVGRKAMFDSDF
HHHHCCCHHHCCCCH		37.97-
221SulfoxidationYYVGRKAMFDSDFKQ
HHCCCHHHCCCCHHH		4.2621406390
227UbiquitinationAMFDSDFKQAEEYLS
HHCCCCHHHHHHHHH		54.30-
232PhosphorylationDFKQAEEYLSFAFEH
CHHHHHHHHHHHHHH		10.1115592455
255 (in isoform 4)Ubiquitination-3.2721890473
258 (in isoform 4)Phosphorylation-6.0127642862
267 (in isoform 4)Ubiquitination-21.0221890473
273 (in isoform 4)Ubiquitination-37.56-
274PhosphorylationTVELLKKYHLMQFAE
HHHHHHHHCHHHHHH		9.9024719451
283PhosphorylationLMQFAEVTRAVSEGN
HHHHHHHHHHHHHCC		12.3820068231
300UbiquitinationLLHEALAKHEAFFIR
HHHHHHHHCHHHHHH		42.71-
383UbiquitinationYISHQHQKLVVSKQN
CCCHHHHHHHEECCC		40.92-
383AcetylationYISHQHQKLVVSKQN
CCCHHHHHHHEECCC		40.9223749302
388UbiquitinationHQKLVVSKQNPFPPL
HHHHHEECCCCCCCC		42.35-
388SumoylationHQKLVVSKQNPFPPL
HHHHHEECCCCCCCC		42.35-
442 (in isoform 4)Ubiquitination--
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PCID2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCID2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PCID2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEM1_HUMANSHFM1physical
22343721
EID1_HUMANEID1physical
24167073
CAPZB_HUMANCAPZBphysical
26344197
DDX3X_HUMANDDX3Xphysical
26344197
IMDH2_HUMANIMPDH2physical
26344197
LSM1_HUMANLSM1physical
26344197
PSMD6_HUMANPSMD6physical
26344197
SNX2_HUMANSNX2physical
26344197
SNX6_HUMANSNX6physical
26344197
UBE4B_HUMANUBE4Bphysical
26344197
VPS35_HUMANVPS35physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCID2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-232, AND MASSSPECTROMETRY.

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